Enzyme Kinetic Analysis with Substrate Inhibition

All graphs were drawn using Prism GraphPad. Michaelis−Menten kinetics data was also calculated using Prism. Substrate inhibition curves were plotted using Prism or the Dynafit software and the equations in Scheme 1 [53 (link)], where Ks and Kss are dissociation constants and kcat is the turnover of the enzyme in min⁻¹. The K_m and V_max were determined using Prism, using points below the substrate inhibition concentrations.

Scheme 1. Mechanism for substrate inhibition. This mechanism assumes that enzyme I has two substrate (S) binding sites: a catalytic site for normal catalysis and a second non-catalytic or allosteric binding site. When substrate is bound at both sites (SES), the product (P) is produced at a reduced rate.

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Batt S.M., Toth S., Rodriguez B., Abrahams K.A., Veerapen N., Chiodarelli G., Cox L.R., Moynihan P.J., Lelievre J., Fütterer K, & Besra G.S. (2023). Assay development and inhibition of the Mt-DprE2 essential reductase from Mycobacterium tuberculosis. Microbiology, 169(1), 001288.

Publication 2023

Binding sites Catalytic Catalytic site Enzyme Inhibition Kinetics Prism

Corresponding Organization :

Other organizations : University of Birmingham, GlaxoSmithKline (Spain)

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Variable analysis

independent variables

Substrate concentration

dependent variables

Enzyme kinetics (Michaelis-Menten parameters Km and Vmax)
Substrate inhibition curves

control variables

Enzyme concentration
Reaction time
Reaction conditions (temperature, pH, etc.)

controls

Positive control: Not explicitly mentioned
Negative control: Not explicitly mentioned

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